Effects of fermented soybean meal on carbon and nitrogen metabolisms in large intestine of piglets.

Fermented soybean meal (FSM), which has lower anti-nutritional factors and higher active enzyme, probiotic and oligosaccharide contents than its unfermented form, has been reported to improve the feeding value of soybean meal, and hence, the growth performance of piglets. However, whether FSM can affect the bacterial and metabolites in the large intestine of piglets remains unknown. This study supplemented wet-FSM (WFSM) or dry-FSM (DFSM) (5% dry matter basis) in the diet of piglets and investigated its effects on carbon and nitrogen metabolism in the piglets' large intestines. A total of 75 41-day-old Duroc×Landrace×Yorkshire piglets with an initial BW of 13.14±0.22 kg were used in a 4-week feeding trial. Our results showed that the average daily gain of piglets in the WFSM and DFSM groups increased by 27.08% and 14.58% and that the feed conversion ratio improved by 18.18% and 7.27%, respectively, compared with the control group. Data from the prediction gene function of Phylogenetic Investigation of Communities by Reconstruction of Unobserved States (PICRUSt) based on 16S ribosomal RNA (rRNA) sequencing showed that carbohydrate metabolism function families in the WFSM and DFSM groups increased by 3.46% and 2.68% and that the amino acid metabolism function families decreased by 1.74% and 0.82%, respectively, compared with the control group. These results were consistent with those of other metabolism studies, which showed that dietary supplementation with WFSM and DFSM increased the level of carbohydrate-related metabolites (e.g. 4-aminobutanoate, 5-aminopentanoate, lactic acid, mannitol, threitol and ß-alanine) and decreased the levels of those related to protein catabolism (e.g. 1,3-diaminopropane, creatine, glycine and inosine). In conclusion, supplementation with the two forms of FSM improved growth performance, increased metabolites of carbohydrate and reduced metabolites of protein in the large intestine of piglets, and WFSM exhibited a stronger effect than DFSM.

[Recombinant human tumor necrosis factor receptor type â ¡-IgG Fc fusion protein for treatment of occupational medicamentosa-like dermatitis induced by trichloroethylene].

Objective: To investigate the efficacy and safety of the recombinant human tumor necrosis factor receptor Ⅱ-IgG Fc fusion protein (rhTNFR: Fc, etanercept) for the treatment of occupational medicamentosa-like dermatitis induced by trichloroethylene (OMLDT) . Methods: In September 2011 to February 2016, 12 patients with OMLDT were treated with etanercept 25 mg, subcutaneous injection, twice per week, doubling of first dose. The course of treatment was 6 weeks. The drug eruption area and severity index (DASI) score, the proportion of patients achieving a 50%, 75% and 90% reduction in DASI (DASI50, DASI75, DASI90) and the serum level of TNF-α were used to assess the efficacy at different times. Adverse reactions were also recorded and evaluated. The results were statistically analyzed by nonparametric Friedman test and repetitive measurement ANOVA using the software SPSS19.0. Results: After 4 weeks treatment, the DASI score decreased form 56.33±7.02 to 0.50±0.91 (P<0.01) . The DASI50, DASI75 and DASI90 were all increased to 12 (100%) . The serum level of TNF-α decreased form (43.74±41.62) pg/ml to (3.03±0.47) pg/ml (P<0.01) . Statistically significant difference was observed from the above indexes. There were no adverse reactions in clinical application. Conclusion: Recombinant human tumor necrosis factor receptor Ⅱ-IgG Fc fusion protein may be a safe and effective drug in the treatment of OMLDT.

Biochemical association of CD45 with the T cell receptor complex: regulation by CD45 isoform and during T cell activation.

CD45 is the predominant transmembrane tyrosine phosphatase in lymphocytes and is required for the efficient induction of T cell receptor signaling and activation. However, the regulation of CD45 activity and substrate specificity are poorly understood. In the present study, we demonstrate a basal biochemical association of CD45 with the T cell receptor complex that is regulated in part by CD45 isoform expression. Further, maintenance of CD45/TCR association is differentially regulated following TCR ligation with peptide: a partial agonist peptide induces CD45/TCR dissociation while an agonist peptide promotes sustained association in a CD4-dependent manner. These data suggest that T cell receptor signaling pathways may be modulated by altering access of CD45 to TCR-associated substrates involved in T cell activation.

CD4 and CD45 regulate qualitatively distinct patterns of calcium mobilization in individual CD4+ T cells.

An early consequence of T cell activation is an increase in intracellular calcium concentration. Recent advances in video laser microscopic techniques enable the examination of individual cells over time following stimulation. Such studies have revealed that cells can undergo qualitatively distinct patterns of calcium mobilization, suggesting that different patterns of calcium flux may be associated with different signaling pathways and may differentially affect late events in cell activation. In this report, we identify distinct patterns of calcium mobilization in CD4+ T cells following the antibody-mediated cross-linking of either CD3 or CD4, or following the cross-linking of both CD3 and CD4 simultaneously. These effects can be further modified by the cross-linking of CD45. We find that antibody cross-linking of CD3 alone induces a single spike in the vast majority of cells shortly after the addition of the cross-linking antibody. In contrast, cross-linking CD4 alone induces a delayed pattern of repetitive calcium spikes which are decreased in amplitude compared to CD3 cross-linking. Simultaneous cross-linking of CD3 and CD4 induces a sustained increase in intracellular calcium mobilization which is dependent on the presence of extracellular calcium. This sustained increase in intracellular calcium concentration is also seen following physiologic cross-linking of CD3 and CD4 after T cell interaction with specific antigen and antigen-presenting cells. Finally, the simultaneous cross-linking of CD45, CD3 and CD4 abrogates the sustained increase in calcium seen following CD3 and CD4 cross-linking. These results suggest that the qualitative nature of T cell receptor signaling can be modulated by the molecular association of other signaling molecules, which may be part of the T cell receptor complex or not.